Evidence map›Paper›PMID 10037792›Full record

ArticleThe Journal of cell biology1999

The yeast dynamin-like protein, Mgm1p, functions on the mitochondrial outer membrane to mediate mitochondrial inheritance.

K A Shepard, M P Yaffe

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
4.5field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

57 citing papers in PubMed, 177 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Structural analysis of a trimeric assembly of the mitochondrial dynamin-like GTPase Mgm1.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  6. Bacterial dynamin-like protein DynA mediates lipid and content mixing.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  7. Article
  8. Article
  9. Article
  10. Mitochondrial division and fusion in metabolism.Current opinion in cell biology · 2015
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. The power of yeast to model diseases of the powerhouse of the cell.Frontiers in bioscience (Landmark edition) · 2013
    Review
  17. Article
  18. Article
  19. Article
  20. The PARL family of mitochondrial rhomboid proteases.Seminars in cell & developmental biology · 2010
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

K A ShepardDepartment of Biology, University of California, San Diego, La Jolla, California 92093-0347, USA.
M P Yaffe
University of California, San Diego · US

Funding

MECHANISMS OF MITOCHONDRIAL DIVISION AND INHERITANCER01GM044614 · NIGMS · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI YAFFE, MICHAEL P. · 1993 to 2004
$1.4M
NIGMS NIH HHS GM44614NIGMS NIH HHS R01 GM044614
6 · The paper itself

Abstract

The mdm17 mutation causes temperature-dependent defects in mitochondrial inheritance, mitochondrial morphology, and the maintenance of mitochondrial DNA in the yeast Saccharomyces cerevisiae. Defects in mitochondrial transmission to daughter buds and changes in mitochondrial morphology were apparent within 30 min after shifting cells to 37 degrees C, while loss of the mitochondrial genome occurred after 4-24 h at the elevated temperature. The mdm17 lesion mapped to MGM1, a gene encoding a dynamin-like GTPase previously implicated in mitochondrial genome maintenance, and the cloned MGM1 gene complements all of the mdm17 mutant phenotypes. Cells with an mgm1-null mutation displayed aberrant mitochondrial inheritance and morphology. A version of mgm1 mutated in a conserved residue in the putative GTP-binding site was unable to complement any of the mutant defects. It also caused aberrant mitochondrial distribution and morphology when expressed at high levels in cells that also contained a wild-type copy of the gene. Mgm1p was localized to the mitochondrial outer membrane and fractionated as a component of a high molecular weight complex. These results indicate that Mgm1p is a mitochondrial inheritance and morphology component that functions on the mitochondrial surface.

Indexed as

GTP-Binding ProteinsMitochondrial ProteinsSaccharomyces cerevisiae ProteinsAllelesBase SequenceBinding SitesConserved SequenceDNA, FungalDNA, MitochondrialDNA PrimersFungal ProteinsGenes, FungalGenome, FungalGuanosine TriphosphateIntracellular MembranesMitochondriaDNA, FungalDNA, MitochondrialDNA PrimersFungal ProteinsGTP-Binding ProteinsGuanosine TriphosphateMGM1 protein, S cerevisiaeMitochondrial ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID10037792
PMCPMC2132935
OpenAlexW2090866135

What OpenQuestion holds

Texttitle and abstract
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.